4QXK
Joint X-ray/neutron structure of PKGIbeta in complex with cGMP
Summary for 4QXK
| Entry DOI | 10.2210/pdb4qxk/pdb |
| Descriptor | cGMP-dependent protein kinase 1, CYCLIC GUANOSINE MONOPHOSPHATE, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | cyclic gmp (cgmp), type i cgmp dependent protein kinase (pkg i), cyclic nucleotide selectivity, serine/threonine protein kinase, signal transduction, second messengers, hydrogen bonding, solvent accessibility, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 17314.01 |
| Authors | Kim, C.,Gerlits, O.,Kovalevsky, A.,Huang, G.Y. (deposition date: 2014-07-21, release date: 2014-11-12, Last modification date: 2024-02-28) |
| Primary citation | Huang, G.Y.,Gerlits, O.O.,Blakeley, M.P.,Sankaran, B.,Kovalevsky, A.Y.,Kim, C. Neutron Diffraction Reveals Hydrogen Bonds Critical for cGMP-Selective Activation: Insights for cGMP-Dependent Protein Kinase Agonist Design. Biochemistry, 53:6725-6727, 2014 Cited by PubMed Abstract: High selectivity of cyclic-nucleotide binding (CNB) domains for cAMP and cGMP are required for segregating signaling pathways; however, the mechanism of selectivity remains unclear. To investigate the mechanism of high selectivity in cGMP-dependent protein kinase (PKG), we determined a room-temperature joint X-ray/neutron (XN) structure of PKG Iβ CNB-B, a domain 200-fold selective for cGMP over cAMP, bound to cGMP (2.2 Å), and a low-temperature X-ray structure of CNB-B with cAMP (1.3 Å). The XN structure directly describes the hydrogen bonding interactions that modulate high selectivity for cGMP, while the structure with cAMP reveals that all these contacts are disrupted, explaining its low affinity for cAMP. PubMed: 25271401DOI: 10.1021/bi501012v PDB entries with the same primary citation |
| Experimental method | NEUTRON DIFFRACTION (2.2 Å) X-RAY DIFFRACTION |
Structure validation
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